An SOS Regulon under Control of a Noncanonical LexA-Binding Motif in the Betaproteobacteria

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dc.contributor.authorSanchez-Alberola, Neus
dc.contributor.authorCampoy, Susana
dc.contributor.authorEmerson, David
dc.contributor.authorBarbé, Jordi
dc.contributor.authorErill, Ivan
dc.date.accessioned2021-03-08T18:09:23Z
dc.date.available2021-03-08T18:09:23Z
dc.date.issued2015-05-18
dc.description.abstractThe SOS response is a transcriptional regulatory network governed by the LexA repressor that activates in response to DNA damage. In the Betaproteobacteria, LexA is known to target a palindromic sequence with the consensus sequence CTGT-N8-ACAG. We report the characterization of a LexA regulon in the iron-oxidizing betaproteobacterium Sideroxydans lithotrophicus. In silico and in vitro analyses show that LexA targets six genes by recognizing a binding motif with the consensus sequence GAACGaaCGTTC, which is strongly reminiscent of the Bacillus subtilis LexA-binding motif. We confirm that the closely related Gallionella capsiferriformans shares the same LexA-binding motif, and in silico analyses indicate that this motif is also conserved in the Nitrosomonadales and the Methylophilales. Phylogenetic analysis of LexA and the alpha subunit of DNA polymerase III (DnaE) reveal that the organisms harboring this noncanonical LexA form a compact taxonomic cluster within the Betaproteobacteria. However, their lexA gene is unrelated to the standard Betaproteobacteria lexA, and there is evidence of its spread through lateral gene transfer. In contrast to other reported cases of noncanonical LexA-binding motifs, the regulon of S. lithotrophicus is comparable in size and function to that of many other Betaproteobacteria, suggesting that a convergent SOS regulon has reevolved under the control of a new LexA protein. Analysis of the DNA-binding domain of S. lithotrophicus LexA reveals little sequence similarity with that of other LexA proteins targeting similar binding motifs, suggesting that network structure may limit site evolution or that structural constrains make the B. subtilis-type motif an optimal interface for multiple LexA sequences.en_US
dc.description.sponsorshipThis study was supported by UMBC Special Research Assistantship/Initiative Support (SRAIS) and U.S. National Science Foundation (MCB-1158056) awards to I.E. and by Spanish Ministry of Science and Innovation (BFU2011-23478) and Generalitat de Catalunya (2014SGR572) awards to J.B. N.S.-A. was funded by a Fundació Cellex fellowship.en_US
dc.description.urihttps://jb.asm.org/content/197/16/2622.longen_US
dc.format.extent9 pagesen_US
dc.genrejournal articlesen_US
dc.identifierdoi:10.13016/m2ybrg-f7xp
dc.identifier.citationSanchez-Alberola N, Campoy S, Emerson D, Barbé J, Erill I. 2015. An SOS regulon under control of a noncanonical LexA-binding motif in the Betaproteobacteria. J Bacteriol 197:2622–2630. doi:10.1128/JB.00035-15en_US
dc.identifier.urihttps://doi.org/10.1128/JB.00035-15
dc.identifier.urihttp://hdl.handle.net/11603/21092
dc.language.isoen_USen_US
dc.publisherAmerican Society for Microbiologyen_US
dc.relation.isAvailableAtThe University of Maryland, Baltimore County (UMBC)
dc.relation.ispartofUMBC Biological Sciences Department Collection
dc.relation.ispartofUMBC Faculty Collection
dc.rightsThis item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.
dc.subjecttranscriptional systemsen_US
dc.subjectnoncanonical LexAen_US
dc.subjectbetaproteobacteriaen_US
dc.subjectmicrobiologyen_US
dc.titleAn SOS Regulon under Control of a Noncanonical LexA-Binding Motif in the Betaproteobacteriaen_US
dc.typeTexten_US

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